The structure and peroxidase activity of myoglobin in alcoholic solvents

被引：5

作者：

Long, Andrew ^{[1
]}

Rothenberg, Paul ^{[1
]}

Patel, Dhea ^{[1
]}

MacDougall, Julia ^{[1
]}

Hartings, Matthew R. ^{[1
]}

机构：

[1] Amer Univ, Dept Chem, 4400 Massachusetts Ave NW, Washington, DC 20016 USA

来源：

POLYHEDRON | 2016年 / 114卷

关键词：

Enzyme catalysis; Organic solvent; Myoglobin; Protein engineering; Peroxidase; ORGANIC-SOLVENTS; HYDROGEN-PEROXIDE; HORSERADISH-PEROXIDASE; ENZYMATIC CATALYSIS; DIRECTED EVOLUTION; DESIGN; METALLOPROTEINS; PROTEINS; ENZYMES; MEDIA;

D O I：

10.1016/j.poly.2015.11.028

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

We present data on the peroxidase activity of equine skeletal myoglobin in water, methanol, ethanol, 1-propanol, 2-propanol, 1-butanol, and 1-pentanol. For experimentation in non-aqueous solvents the protein structure was stabilized through lyophilization from a solution of a buffer and 98% (dry weight) KCl. Myoglobin showed some solubility in methanol and its structure was probed with circular dichroism and UV Vis absorption spectroscopies. Peroxidase activity of myoglobin toward the oxidation of o-phenylenediamine to 2,3-diaminophenazine was observed and measured in each of the listed solvents. The system in methanol showed the fastest initial rate of reaction. This initial rate in the other organic solvents was similar to the rate in water. However, myoglobin showed stable catalysis for a longer period of time in water. These results provide a first step forward in guiding the utilization of re-engineered myoglobin variants in non-aqueous solvents. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：138 / 144

页数：7

共 48 条

[31] Expanding the Enzyme Universe: Accessing Non-Natural Reactions by Mechanism-Guided Directed Evolution
Renata, Hans
Wang, Z. Jane
Arnold, Frances H.
[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2015, 54 (11) : 3351 - 3367
[32] Enzyme architecture: on the importance of being in a protein cage
Richard, John P.
Amyes, Tina L.
Goryanova, Bogdana
Zhai, Xiang
[J]. CURRENT OPINION IN CHEMICAL BIOLOGY, 2014, 21 : 1 - 10
[33] RodriguezLopez JN, 1996, J BIOL CHEM, V271, P4023
[34] Towards more active biocatalysts in organic media: Increasing the activity of salt-activated enzymes
Ru, MT
Wu, KC
Lindsay, JP
Dordick, JS
Reimer, JA
Clark, DS
[J]. BIOTECHNOLOGY AND BIOENGINEERING, 2001, 75 (02) : 187 - 196
[35] Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins
Saven, Jeffery G.
[J]. CURRENT OPINION IN CHEMICAL BIOLOGY, 2011, 15 (03) : 452 - 457
[36] Enzyme activation for organic solvents made easy
Serdakowski, Anne L.
Dordick, Jonathan S.
[J]. TRENDS IN BIOTECHNOLOGY, 2008, 26 (01) : 48 - 54
[37] The Outer-Coordination Sphere: Incorporating Amino Acids and Peptides as Ligands for Homogeneous Catalysts to Mimic Enzyme Function
Shaw, Wendy J.
[J]. CATALYSIS REVIEWS-SCIENCE AND ENGINEERING, 2012, 54 (04): : 489 - 550
[38] Biochemical Properties and Potential Applications of a Solvent-Stable Protease from the High-Yield Protease Producer Pseudomonas aeruginosa PT121
Tang, Xiao-Yu
Wu, Bin
Ying, Han-Jie
He, Bing-Fang
[J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2010, 160 (04) : 1017 - 1031
[39] Triantafyllou AO, 1997, BIOTECHNOL BIOENG, V54, P67, DOI 10.1002/(SICI)1097-0290(19970405)54:1<67::AID-BIT8>3.0.CO
[40] 2-W

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